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Literature summary for 2.7.2.2 extracted from

  • Ramon-Maiques, S.; Marina, A.; Uriarte, M.; Fita, I.; Rubio, V.
    The 1.5 A resolution crystal structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic Archaeon pyrococcus furiosus, bound to ADP, confirms that this thermostable enzyme is a carbamate kinase, and provides insight into substrate binding and stability in carbamate kinases (2000), J. Mol. Biol., 299, 463-476.
    View publication on PubMed
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Crystallization (Commentary)

Crystallization (Comment) Organism
-
 Pyrococcus furiosus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.001
-
 ADP pH 8.0, 37°C Pyrococcus furiosus
0.017
-
 ATP pH 8.0, 37°C Pyrococcus furiosus

Organism

Organism UniProt Comment Textmining
Pyrococcus furiosus P95474
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + NH3 + hydrogencarbonate = ADP + carbamoyl phosphate + H2O mechanism Pyrococcus furiosus
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP + carbamoyl phosphate
-
 Pyrococcus furiosus ATP + NH3 + CO2
-
 r
ATP + NH3 + CO2 carbamoyl phosphate synthetase is a carbamate synthase Pyrococcus furiosus ADP + carbamoyl phosphate
-
 r

Subunits

Subunits Comment Organism
dimer homodimer, crystalline structure Pyrococcus furiosus